A novel KH-domain protein mediates cell adhesion processes in Drosophila
A novel KH-domain protein mediates cell adhesion processes in Drosophila
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DOI：
10.1006/dbio.1997.8699
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发表时间：
1997-10-15
影响因子：
2.7
通讯作者：
Frasch, M
中科院分区：
文献类型：
--
作者：
Lo, PCH;Frasch, M
细胞相互粘附和细胞外基质粘附在发育过程中的形态发生过程中起着重要作用。细胞粘附受体的一个重要家族是整合素，其在果蝇中至少在两个粘附介导的发育事件中具有关键功能：胚胎肌肉附着和翼上皮的粘附。我们已经克隆并表征了一个基因（struthio），该基因在胚胎中胚层和肌肉细胞，包括成心细胞和表皮肌肉附着位点中表达，其模式让人想起PS整合素的表达模式。母体和合子转录本由该基因产生，并编码具有两个交替羧基尾的相似蛋白质。两种蛋白质都含有相同的KH结构域，这是一种在许多与RNA相互作用的蛋白质中发现的蛋白质序列基序。该struthio蛋白在包括KH结构域的区域中与小鼠震颤和C. elegans gld-1蛋白，两个发育重要的基因。该基因（stru（1A 122））中胚胎致死突变的体细胞纯合克隆引起翅水泡和夜间障碍，这些表型与PS整联蛋白亚基突变相关。因此，struthio基因编码一个假定的RNA结合蛋白，似乎调节果蝇整合素功能的某些方面。(C)北京：科学出版社.
Adhesion of cells to one another and to extracellular matrices has major roles in morphogenetic processes during development. One important family of cell adhesion receptors are the integrins, which in Drosophila have crucial functions in at least two adhesion-mediated developmental events: embryonic muscle attachment and adhesion of the wing epithelia. We have cloned and characterized a gene (struthio) that is expressed in embryonic mesodermal and muscle cells, including cardioblasts, and epidermal muscle attachment sites in a pattern that is reminiscent of the expression pattern of the PS integrins. Maternal and zygotic transcripts are produced by this gene and encode similar proteins with two alternative carboxy tails. Both proteins contain identical KH domains, a protein sequence motif that is found in numerous proteins that interact with RNA. The struthio protein is highly homologous in a region including the KH domain to the mouse quaking and C. elegans gld-1 proteins, two developmentally important genes. Somatic homozygous clones of an embryonic lethal mutation in this gene (stru(1A122)) cause wing blisters and night impairment, phenotypes which are associated with PS integrin subunit mutations. Thus, the struthio gene encodes a putative RNA-binding protein that appears to regulate some aspects of Drosophila integrin functioning. (C) 1997 Academic Press.